This chapter reviews and discusses various aspects of texture analysis. The concentration is o the various methods of extracting textural features from images. The geometric, random field, fractal, and signal processing models of texture are presented. The major classes of texture processing pro lems such as segmentation, classification, and shape from texture are discussed. The possible applic tion areas of texture such as automated inspection, document processing, and remote sensing a summarized. A bibliography is provided at the end for further reading.

Texture analysis

This study characterizes biologically active compounds of berry fruits, including non-nutritive compounds such as phenolic compounds, including anthocyanins, phenolic acids, stilbens and tannins, as well as nutritive compounds such as carotenoids and vitamin C. It discusses the biological activity of those compounds, in particular their antioxidant properties and the resulting health benefits.

Bioactive compounds and health-promoting properties of berry fruits: a review.

References.- 1 Solubility of Proteins.- 1.1 Introduction.- 1.1.1 Factors Affecting Solubility of Proteins.- 1.2 Solubility of Meat and Fish Proteins.- 1.2.1 Solubility of Muscle Proteins.- 1.2.2 Solubility of Stroma Proteins.- 1.2.3 Protein Solubility in Processed Meats.- 1.2.4 Solubility of Blood Proteins.- 1.2.5 The Effect of Heating on Solubility of Proteins.- 1.2.6 The Effect of Freezing and Storage When Frozen on Protein Solubility.- 1.2.7 The Effect of Protein Modification and Irradiation Treatment.- 1.3 Solubility of Milk Proteins.- 1.4 Solubility of Egg Proteins.- 1.5 Solubility of Plant Proteins.- 1.5.1 Soybean Proteins.- 1.5.2 Peanut Proteins.- 1.5.3 Pea and Bean Proteins.- 1.5.4 Sunflower Proteins.- 1.5.5 Corn Proteins.- 1.5.6 Miscellaneous Plant Proteins.- References.- 2 Water Holding Capacity of Proteins.- 2.1 Introduction.- 2.2 The Mechanism of Protein-Water Interaction.- 2.2.1 Factors Influencing Water Binding of Proteins.- 2.3 Water Holding Capacity of Proteins in Meat and Meat Products.- 2.3.1 Water Binding Capacity of Muscle Proteins.- 2.3.2 Factors Influencing Water Binding of Muscle Proteins.- 2.3.3 Water Binding in Comminuted Meat Products.- 2.3.4 Milk Proteins in Comminuted Meats.- 2.3.5 Soy Proteins in Comminuted Meats.- 2.3.6 Corn Germ Protein in Comminuted Meats.- 2.4 Water Holding Capacity of Milk Proteins.- 2.5 Water Holding Capacity of Egg Proteins.- 2.6 Water Holding Capacity of Plant Proteins.- 2.6.1 Soybean Proteins.- 2.6.2 Pea and Bean Proteins.- 2.6.3 Sunflower Proteins.- 2.6.4 Corn Proteins.- 2.6.5 Wheat Proteins.- 2.6.6 Miscellaneous Proteins.- References.- 3 Emulsifying Properties of Proteins.- 3.1 Introduction.- 3.2 Hydrophobic and Hydrophilic Properties of Proteins.- 3.3 Interfacial Film Formation and Properties.- 3.4 Factors Affecting the Emulsifying Properties of Proteins.- 3.4.1 Protein Concentration.- 3.4.2 pH of Medium.- 3.4.3 Ionic Strength.- 3.4.4 Heat Treatment and Other Factors.- 3.5 Emulsion Stability.- 3.6 Measuring Emulsifying Properties.- 3.7 Emulsifying Properties of Meat Proteins and Proteins Utilized as Extenders in Meat Products.- 3.7.1 Protein Functionality in Comminuted Meats.- 3.7.2 Emulsifying Properties of Various Muscular Proteins.- 3.7.3 Emulsifying Properties of Blood Proteins.- 3.8 Functionality of Nonmeat Proteins in Comminuted Meats.- 3.8.1 Milk Proteins.- 3.8.2 Soy Proteins.- 3.8.3 Corn and Wheat Germ Proteins.- 3.9 Milk Proteins as Emulsifiers in Food Systems.- 3.9.1 Emulsifying Properties of Caseins and Caseinates.- 3.9.2 Emulsifying Properties of Whey Proteins.- 3.10 Emulsifying Properties of Egg Proteins.- 3.11 Emulsifying Properties of Plant Proteins.- 3.11.1 Soybean Proteins.- 3.11.2 Pea and Bean Proteins.- 3.11.3 Corn Proteins.- 3.11.4 Miscellaneous Proteins.- References.- 4 Oil and Fat Binding Properties Of Proteins.- 4.1 Introduction.- 4.2 Fat Binding Properties of Proteins of Animal Origin.- 4.2.1 Muscle Proteins.- 4.2.2 Soy Proteins in Comminuted Meats.- 4.2.3 The Effect of Corn Germ Protein Flour on Fat Binding in Ground Beef Patties.- 4.2.4 Milk and Egg Proteins.- 4.3 Fat Binding Properties of Proteins of Plant Origin.- 4.3.1 Soy Proteins.- 4.3.2 Pea, Bean and Guar Proteins.- 4.3.3 Corn Germ Proteins.- 4.3.4 Wheat Proteins.- 4.3.5 Cottonseed Proteins.- 4.3.6 Miscellaneous Proteins.- References.- 5 Foaming Properties of Proteins.- 5.1 Introduction.- 5.2 The Mechanism of Foam Formation.- 5.2.1 Factors Affecting Foam Formation.- 5.2.2 Foam Stability.- 5.3 Milk Proteins.- 5.3.1 Factors Affecting the Foaming Properties of Milk Proteins.- 5.4 Egg Proteins.- 5.4.1 The Effect of Processing on Foaming Properties of Egg Proteins.- 5.5 Blood Proteins and Gelatin.- 5.6 The Foaming Properties of Plant Proteins.- References.- 6 Gelling Properties of Proteins.- 6.1 Introduction.- 6.2 The Mechanism of Protein Gel Formation.- 6.2.1 Heat-Induced Gelation.- 6.2.2 Protein-Water Interaction in Gels.- 6.2.3 Factors Affecting the Properties of Gels.- 6.3 Gelling Properties of Meat Proteins.- 6.3.1 Myofibrillar Proteins.- 6.3.2 Sarcoplasmic Proteins.- 6.3.3 Gelation of Red and White Muscle Proteins.- 6.3.4 Factors Affecting the Gelling Properties of Meat Proteins.- 6.3.5 Myosin Blends with Other Proteins and Lipids.- 6.3.6 Fish Proteins.- 6.3.7 Collagen Gelation.- 6.3.8 Blood Proteins.- 6.4 Gelling Properties of Milk Proteins.- 6.4.1 Gelling Properties of Whey Protein Concentrate, Isolate, and Individual hey Proteins.- 6.4.2 The Effect of Heating and Protein Concentration.- 6.4.3 Gelation of Casein.- 6.4.4 Factors Affecting the Gelling Properties of Milk Proteins.- 6.5 Gelling Properties of Egg Proteins.- 6.5.1 Gelation of Egg White.- 6.5.2 Gelation of Yolk.- 6.6 Gelling Properties of Soy Proteins.- References.

Functionality of Proteins in Food

Where is MAP Going? A review and future potential of modified atmosphere packaging for meat

Proteins are widely utilized to add functional properties, such as gelling and emulsification to foods. These attributes depend on a number of factors such as molecular structure of the protein, the pH, and the composition of its chemical environment. There is substantial evidence to suggest that the functional properties of food proteins can be further improved by derivatization. Covalent bonding of proteins to polysaccharides and smaller reducing sugars via the Maillard reaction has been shown to alter the functionality of proteins without requiring the addition of chemical reagents. Establishment of a technologically feasible method for preparing the conjugates and optimization of the processing conditions, however, is needed to promote their development as functional food ingredients. This paper provides a state-of-the-art contribution to the impact of the Maillard reaction on protein functionality. It presents a deeper understanding of the influence of processing conditions and reactant formulation on improving desirable properties of proteins. In particular attention is given to how potential improvements could be achieved in the emulsifying, textural, and solubility properties of proteins to add value to commodity food ingredients. Elements that are considered to be critical to the design of functional Maillard conjugates are highlighted and suggestions proposed to facilitate progress in this area.

Creating Proteins with Novel Functionality via the Maillard Reaction: A Review

Paper No. FSR-03-40 of the Journal Series of the Department of Food Science, North Carolina State University, Raleigh, NC 27695-7624.

/pdf/gelling-properties-of-atlantic-croaker-surimi-processed-by-lkvnguuyg5.pdf

Gelling properties of Atlantic croaker surimi processed by acid or alkaline solubilization.

Metmyoglobin (Mb+) reduction was studied in ground beef, beef slurries and extracts held in air, nitrogen or CO-air mixtures. Significant Mb+ reduction occurred in aerobic extracts but not in ground beef or slurries in the presence of ferricyanide. A nonenzymatic electron trans. fer was demonstrated in extracts under these conditions. At normal meat pH (5.6), carbon monoxide (CO) accelerated Mb+ reduction, even in the presence of air, with the rate of reduction dependent upon CO concentration. Neither the addition of catalase nor compounds that inhibit the electron transport chain markedly affected Mb+ reduction under a CO atmosphere while arsenate addition slightly accelerated the reaction. The use of ferricyanide as the pigment oxidant increased the Mb+ reduction rate in aerobic extracts and in all systems under CO, but was not necessary to observe reduction under CO. Possible mechanisms for the CO-enhanced reduction of Mb+ are explored.

Metmyoglobin reduction in beef systems as affected by aerobic, anaerobic and carbon monoxide‐containing environments

Heat stable protease isolated from the sarcoplasmic fraction of menhaden (Brevoorti tyrannus) muscle tissue was characterized as to optimum temperature and pH against casein substrate and its degradative action on actomyosin and surimi during heating. The optimum conditions for activity were 60°C at a pH of 7.5 to 8.0. Activity dropped off remarkably at temperatures below 45°C or above 70°C and when pH was below 7.0 or above 8.0. The enzyme(s) was capable of degrading actomyosin as observed by sodium dodecyl sulfate electrophoresis. This implicated a causative role for this protease system in the texture degradation observed during thermal processing of menhaden surimi at temperatures of 50-70°C.

Effects of Heat‐Stable Alakaline Protease Activity of Atlantic Menhaden (Brevootii tyrannus) on Surimi Gels

An alkaline protease was partially purified from the skeletal muscle of Atlantic croaker. The protease is a cytoplasmic enzyme and heat stable. The enzyme preparation was shown to degrade fish actomyosin in vitro between 50–60°C. The enzyme is a sulfhydryl protease and does not require Ca++ ions for its activity. Preparations of the enzyme do not hydrolyze TAME, BTEE or denatured hemoglobin. Column chromatographic analyses suggest an apparent molecular weight of 80,000 ± 4,000 and the isoelectric point is 6.0 ± 0.2.

Tyre C. Lanier

Papers

Gelling properties of Atlantic croaker surimi processed by acid or alkaline solubilization.

Metmyoglobin reduction in beef systems as affected by aerobic, anaerobic and carbon monoxide‐containing environments

Effects of Heat‐Stable Alakaline Protease Activity of Atlantic Menhaden (Brevootii tyrannus) on Surimi Gels

Properties of an alkaline protease from the skeletal muscle of atlantic croaker1

Chicken plasma protein affects gelation of surimi from bigeye snapper (Priacanthus tayenus)